Rhizobium meliloti adenylate cyclase is related to eucaryotic adenylate and guanylate cyclases

A gene from Rhizobium meliloti coding for an adenylate cyclase was sequenced, and the deduced protein sequence was compared with those of other known adenylate cyclases. No similarity could be detected with the procaryotic counterparts. However, striking similarity was found with the catalytic regio...

Full description

Saved in:
Bibliographic Details
Published in:Journal of Bacteriology 1990-05, Vol.172 (5), p.2614-2621
Main Authors: Beuve, A. (Institut Pasteur, Paris, France), Boesten, B, Crasnier, M, Danchin, A, O'Gara, F
Format: Article
Language:English
Subjects:
Adenylyl Cyclases - genetics
Adenylyl Cyclases - metabolism
Amino Acid Sequence
Animals
Base Sequence
beta-Galactosidase - genetics
beta-Galactosidase - metabolism
Biological and medical sciences
Cattle
Chromosome Deletion
Cloning, Molecular
Escherichia coli - genetics
Fundamental and applied biological sciences. Psychology
GENE
GENES
Genes, Bacterial
Genes. Genome
Genotype
Guanylate Cyclase - genetics
LIASAS
LYASE
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
NUCLEOTIDE
NUCLEOTIDOS
Plasmids
Rats
Restriction Mapping
RHIZOBIUM
Rhizobium - enzymology
Rhizobium - genetics
SACCHAROMYCES CEREVISIAE
Saccharomyces cerevisiae - enzymology
Saccharomyces cerevisiae - genetics
Sequence Homology, Nucleic Acid
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:A gene from Rhizobium meliloti coding for an adenylate cyclase was sequenced, and the deduced protein sequence was compared with those of other known adenylate cyclases. No similarity could be detected with the procaryotic counterparts. However, striking similarity was found with the catalytic region of Saccharomyces cerevisiae adenylate cyclase, the cytoplasmic domains of bovine adenylate cyclase, and two mammalian guanylate cyclases. The gene was fused to the enteric beta-galactosidase, and the chimeric protein was purified by affinity chromatography. This fusion protein was found to direct the synthesis of cyclic AMP in vitro. This activity was strongly inhibited by the presence of GTP, but no cyclic GMP synthesis could be detected in conditions permitting cyclic AMP synthesis
ISSN:0021-9193
1098-5530
1067-8832
DOI:10.1128/jb.172.5.2614-2621.1990